(Q34279340)

1 August 2017

Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution (English)

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1 August 2017

Dideberg O

1

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1 August 2017

Charlier P

2

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1 August 2017

Dive G

3

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1 August 2017

Joris B

4

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1 August 2017

Frère JM

5

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1 August 2017

Ghuysen JM

6

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1 August 2017

language of work or name

English

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publication date

1 September 1982

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1 August 2017

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1 August 2017

299

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1 August 2017

469-470

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1 August 2017

5882

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https://scigraph.springernature.com/pub.10.1038/299469a0

1 August 2017

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cites work

Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.

1 reference

Penicillins and cephalosporins are active site-directed acylating agents: evidence in support of the substrate analogue hypothesis

21 January 2018

1 reference

7 January 2021

The exocellular DD-carboxypeptidase of Streptomyces albus G: a metallo (Zn2+) enzyme

1 reference

7 January 2021

Crystallographic data for the dd-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus G

1 reference

7 January 2021

Structural patterns in globular proteins

1 reference

7 January 2021

Handedness of crossover connections in beta sheets

1 reference

7 January 2021

The 4.5 A resolution structure analysis of the exocellular DD-carboxypeptidase of Streptomyces albus G

1 reference

7 January 2021

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7 January 2021

Substrate requirements of the Streptomyces albus G DD carboxypeptidase

1 reference

7 January 2021

The extension of the isomorphous replacement method to include anomalous scattering measurements

1 reference

19 October 2022

https://opencitations.net/index/coci/api/v1/citations/10.1107/S0365110X6600015X

Identifiers

DOI

10.1038/299469A0

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Dimensions Publication ID

1 August 2017

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